› 1h93

X-ray diffraction
2.2Å resolution

ACTIVE MUTANT (S215->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES

Released:
DOI: 10.2210/pdb1h93/pdb
PDB entry 1h93 coloured by chain, front view.
PDB entry 1h93 coloured by chain, side view.
PDB entry 1h93 coloured by chain, top view.
Source organism: Leuconostoc mesenteroides
Primary publication:
NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes.
Naylor CE, Gover S, Basak AK, Cosgrove MS, Levy HR, Adams MJ
Acta Crystallogr D Biol Crystallogr 57 635-48 (2001)
PMID: 11320304

Function and Biology Details

Reaction catalysed: 
D-glucose 6-phosphate + NAD(P)(+) = 6-phospho-D-glucono-1,5-lactone + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145818 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-6-phosphate 1-dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 485 amino acids
Theoretical weight: 54.39 KDa
Source organism: Leuconostoc mesenteroides
Expression system: Escherichia coli
UniProt:
  • Canonical: P11411 (Residues: 2-486; Coverage: 100%)
Gene name: zwf
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: C2
Unit cell:
a: 129.33Å b: 44.28Å c: 91.17Å
α: 90° β: 105.39° γ: 90°
R-values:
R R work R free
0.206 0.206 0.282
Expression system: Escherichia coli

Quick links

Citations

13 citation in other articles

Different biochemical mechanisms ensure network-wide balancing of reducing equivalents in microbial metabolism.
Fuhrer et al. (2009)
12 more